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Three-fluorophore FRET enables the analysis of ternary protein association in living plant cells

Protein-protein interaction studies provide valuable insights into cellular signaling. Brassinosteroid (BR) signaling is initiated by the hormone-binding receptor Brassinosteroid Insensitive 1 (BRI1) and its co-receptor BRI1 Associated Kinase 1 (BAK1). BRI1 and BAK1 were shown to interact independen...

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Main Authors: Glöckner, Nina (Author) , Zur Oven-Krockhaus, Sven (Author) , Rohr, Leander (Author) , Wackenhut, Frank (Author) , Burmeister, Moritz (Author) , Wanke, Friederike (Author) , Holzwart, Eleonore (Author) , Meixner, Alfred J. (Author) , Wolf, Sebastian (Author) , Harter, Klaus (Author)
Format: Article (Journal)
Language:English
Published: 6 October 2022
In: Plants
Year: 2022, Volume: 11, Issue: 19, Pages: 1-18
ISSN:2223-7747
DOI:10.3390/plants11192630
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3390/plants11192630
Verlag, lizenzpflichtig, Volltext: https://www.mdpi.com/2223-7747/11/19/2630
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Author Notes:Nina Glöckner, Sven zur Oven-Krockhaus, Leander Rohr, Frank Wackenhut, Moritz Burmeister, Friederike Wanke, Eleonore Holzwart, Alfred J. Meixner, Sebastian Wolf an Klaus Harter
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Summary:Protein-protein interaction studies provide valuable insights into cellular signaling. Brassinosteroid (BR) signaling is initiated by the hormone-binding receptor Brassinosteroid Insensitive 1 (BRI1) and its co-receptor BRI1 Associated Kinase 1 (BAK1). BRI1 and BAK1 were shown to interact independently with the Receptor-Like Protein 44 (RLP44), which is implicated in BRI1/BAK1-dependent cell wall integrity perception. To demonstrate the proposed complex formation of BRI1, BAK1 and RLP44, we established three-fluorophore intensity-based spectral Förster resonance energy transfer (FRET) and FRET-fluorescence lifetime imaging microscopy (FLIM) for living plant cells. Our evidence indicates that RLP44, BRI1 and BAK1 form a ternary complex in a distinct plasma membrane nanodomain. In contrast, although the immune receptor Flagellin Sensing 2 (FLS2) also forms a heteromer with BAK1, the FLS2/BAK1 complexes are localized to other nanodomains. In conclusion, both three-fluorophore FRET approaches provide a feasible basis for studying the in vivo interaction and sub-compartmentalization of proteins in great detail.
Item Description:Gesehen am 04.01.2023
Physical Description:Online Resource
ISSN:2223-7747
DOI:10.3390/plants11192630

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